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Dynamic pH‐induced conformational changes of the PsbO protein in the fluctuating acidity of the thylakoid lumen
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Charles University, Prague, Czech Republic.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Vise andre og tillknytning
2019 (engelsk)Inngår i: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 166, nr 1, s. 288-299Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The PsbO protein is an essential extrinsic subunit of photosystem II, the pigment–protein complex responsible for light‐driven water splitting. Water oxidation in photosystem II supplies electrons to the photosynthetic electron transfer chain and is accompanied by proton release and oxygen evolution. While the electron transfer steps in this process are well defined and characterized, the driving forces acting on the liberated protons, their dynamics and their destiny are all largely unknown. It was suggested that PsbO undergoes proton‐induced conformational changes and forms hydrogen bond networks that ensure prompt proton removal from the catalytic site of water oxidation, i.e. the Mn4CaO5 cluster. This work reports the purification and characterization of heterologously expressed PsbO from green algae Chlamydomonas reinhardtii and two isoforms from the higher plant Solanum tuberosum (PsbO1 and PsbO2). A comparison to the spinach PsbO reveals striking similarities in intrinsic protein fluorescence and CD spectra, reflecting the near‐identical secondary structure of the proteins from algae and higher plants. Titration experiments using the hydrophobic fluorescence probe ANS revealed that eukaryotic PsbO proteins exhibit acid–base hysteresis. This hysteresis is a dynamic effect accompanied by changes in the accessibility of the protein's hydrophobic core and is not due to reversible oligomerization or unfolding of the PsbO protein. These results confirm the hypothesis that pH‐dependent dynamic behavior at physiological pH ranges is a common feature of PsbO proteins and causes reversible opening and closing of their β‐barrel domain in response to the fluctuating acidity of the thylakoid lumen.

sted, utgiver, år, opplag, sider
John Wiley & Sons, 2019. Vol. 166, nr 1, s. 288-299
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Identifikatorer
URN: urn:nbn:se:umu:diva-157462DOI: 10.1111/ppl.12948ISI: 000466108300023PubMedID: 30793329OAI: oai:DiVA.org:umu-157462DiVA, id: diva2:1297785
Forskningsfinansiär
The Kempe FoundationsKnut and Alice Wallenberg Foundation, KAW2011.0055
Merknad

Special Issue: SI

Tilgjengelig fra: 2019-03-21 Laget: 2019-03-21 Sist oppdatert: 2019-06-10bibliografisk kontrollert

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Carius, Anke B.Rogne, PerWolf-Watz, MagnusSamuelsson, GöranShutova, Tatiana

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